Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrial inner membrane | the enzyme is found in monomeric, dimeric and higher oligomeric forms in the inner mitochondrial membrane. Two small proteins of the membrane-embedded Fo-domain subunits e and g are dimer-specific subunits of yeast ATP synthase and are required for stabilization of the dimers | Saccharomyces cerevisiae | 5743 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Saccharomyces cerevisiae |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O + H+/in | Saccharomyces cerevisiae | - |
ADP + phosphate + H+/out | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + H2O + H+/in | - |
Saccharomyces cerevisiae | ADP + phosphate + H+/out | - |
r |
Subunits | Comment | Organism |
---|---|---|
More | the enzyme is found in monomeric, dimeric and higher oligomeric forms in the inner mitochondrial membrane. Dimerization of ATP synthase complexes is a prerequisite for the generation of larger oligomers that promote membrane bending and formation of tubular cristae membranes. Two small proteins of the membrane-embedded Fo-domain subunits e and g are dimer-specific subunits of yeast ATP synthase and are required for stabilization of the dimers. Subunits e and g sequentially assemble with monomeric ATP synthase to form a dimerization-competent primed monomer, overview | Saccharomyces cerevisiae |
Synonyms | Comment | Organism |
---|---|---|
ATP synthase | - |
Saccharomyces cerevisiae |
mitochondrial F1Fo-ATP synthase | - |
Saccharomyces cerevisiae |